2. Parapoptosis

3. Apaf-1 independent as well as cytochrome c

4. Does not activate caspase 9 via apaf-1

5. It activates an alternative caspase

6. ECM

7. Muscle

8. Nervous

9. Connective

10. types

11. Bone

12. Cells secrete ECM

13. Osteocytes

14. Mature cells of this cell type

15. Osteoblast – secretes ECM of molecules

16. Cartilage

17. Chrondrocytes

18. Mature cells of this cell type

19. Chrondroblasts

20. Secrete ECM of Cartilage

21. Loose connective tissue (under epithelium)

22. Blood

23. Lymphoid tissue

24. More ECM than cells

25. Epithelial Tissue more ECM than cells

26. Independent of connective tissue

27. Made of epithelial cells

28. Attach to basil lamina

29. Fibroblasts

30. Loose connective tissue

31. Skin

32. Epithelial cells

33. Linked by tight junctions to integrins

34. Underneath is loose connective tissue that proveide tensile strength

35. ECM of Loose connective Tissue

36. Proteoglycans

37. Made up of a core protein linked to many negatively charged polysaccharides that have a particular structure

38. This structure characterizes them as GAGS – glycosoaminoglycans

39. Negative charges attracts water

40. Now the ECM has a fluid-like component to it.

41. Presence of proteoglycans will determine how fluid the ECM is (bones don’t have much)

42. Fibrillar

43. Types

44. Collagen

45. Fibronectin

46. Elastin

47. Provides

48. Strength

49. Attachment sites for cell receptors

50. Collagen

51. Characterized by alpha subunit

52. Can combine in different ways to produce the different collagens

53. Synthesis of Collagen

54. Occurs in the ER lumen

55. Contain

56. Prolin

57. Heavily hydroxylated – form H bonds as single alpha chains come to form a triple helix between hydroxylated prolin

58. Hydroxylated lysine are also involved

59. Scurvy

60. Decrease in hydroxylated proline levels

61. Lack of vitamin c

62. Helps hydroxlate prolin

63. Glycine

64. Smallest amino acid

65. Every 3rd amino acid in a collagen chain is a glycine

66. Allows close interaction of chains to favor the formation of hydrogen bonds

67. Forms a fibril, about 270, are aligned so they overlap in a region ~ 67nm wide

68. Once fibrils assemble into a fiber, they are striated in form because of how the collagen molecule is offset. This allows tensile strength. This is a phenotype of the collagen and why it has a strong tensile strength

69. Type-1 Collagen

70. Tendons

71. Cornea of eye

72. ~95% of collagen in body

73. Type-1 fiber

74. Interaction between type 1 and type 4 allows a molecule that is rigid and flexible.

75. Mutations in Type-1

76. Usually heavily localized in bons

77. Osteogenesis imperfecta

78. Genetic, makes bones brittle.

79. Mutaions in Type-II

80. Chondrodisplasiaa

81. This collagen is heavily found in cartilage

82. Mutations in Type-III Collagen

83. Ehler-Danlos syndrome

84. Attachment of blood vessels and joints

85. Skin is fragile

86. Joints are hypermobile, blistering, skin rupturing.

87. Type-II Fibril Structure

88. Tye-II fibril

89. Associates with type-IX with flexible kinks

90. As It assembles, primarily in cartilage, n terminus stick out, so the space generated organizes collagen so it crisscrosses, and inbetween are proteoglycans, creates gel liked structure of cartilage

91. Proline

92. Disease

93. Rheumatoid Arthritis

94. Immune system attacks collagen

95. Normally collagen is not immunogenic

96. Fibronectin

97. Secreted by fibroblasts

98. Important roles out in the connective tissue to help organize connective tissue

99. Made of two large polypeptides

100. At COOH terminus, linked by di sulfide bonds to hold the polypeptides together

101. Binding sites on fibronetin

102. Blood clotting

103. Fibrin binding domain

104. Heparin

105. Arginine, glycine, asartate – form RGD sequence

106. Used for integrin receptors

107. Collagen Binding Domain

108. Heparin and fibrin

109. Integrins nteractct with fibronectin in connective tissue

110. Proteoglycans and Glycosaminoglycans

111. Chrondroitin Sulfate

112. Keratin Sulfate

113. Hyalurnoate

114. Don’t memorize the combinations of sugars, just know that there are different combinations of sugars to make different compounds.

115. Aggrecan

116. Core protein is heavily concentrated with hyalurnate

117. Proteoglycans stick of hyal molecule

118. Hyal organizes the prot glycs

119. Found in cartilage

120. Integrins

121. Alpha and beta chain

122. Can vary

123. Which can yield a specific function for that integrin

124. A7b1 – muscular distrophy